1PT2
Crystal structure of levansucrase (E342A) complexed with sucrose
Summary for 1PT2
Entry DOI | 10.2210/pdb1pt2/pdb |
Related | 1OYG |
Related PRD ID | PRD_900003 |
Descriptor | Levansucrase, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
Functional Keywords | glycoside hydrolase, levansucrase, beta-propeller, levan, sucrose, transferase |
Biological source | Bacillus subtilis |
Cellular location | Secreted: P05655 |
Total number of polymer chains | 1 |
Total formula weight | 50646.96 |
Authors | Meng, G.,Futterer, K. (deposition date: 2003-06-22, release date: 2003-10-14, Last modification date: 2023-08-16) |
Primary citation | Meng, G.,Futterer, K. Structural framework of fructosyl transfer in Bacillus subtilis levansucrase Nat.Struct.Biol., 10:935-941, 2003 Cited by PubMed Abstract: Many bacteria and about 40,000 plant species form primary carbohydrate reserves based on fructan; these polymers of beta-D-fructofuranose are thought to confer tolerance to drought and frost in plants. Microbial fructan, the beta(2,6)-linked levan, is synthesized directly from sucrose by levansucrase, which is able to catalyze both sucrose hydrolysis and levan polymerization. The crystal structure of Bacillus subtilis levansucrase, determined to a resolution of 1.5 A, shows a rare five-fold beta-propeller topology with a deep, negatively charged central pocket. Arg360, a residue essential for polymerase activity, lies in a solvent-exposed site adjacent to the central pocket. Mutagenesis data and the sucrose-bound structure of inactive levansucrase E342A, at a resolution of 2.1 A, strongly suggest that three conserved acidic side chains in the central pocket are critical for catalysis, and presumably function as nucleophile (Asp86) and general acid (Glu342), or stabilize the transition state (Asp247). PubMed: 14517548DOI: 10.1038/nsb974 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
